Structural highlights
Function[LDI_CASDE] Anaerobically catalyzes the stereospecific hydration of beta-myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol. Is thus involved in the initial steps of the anaerobic degradation of the monoterpene beta-myrcene. Also catalyzes the reverse reactions, i.e. the isomerization of geraniol to linalool and the dehydration of linalool to myrcene. In this direction, the formation of myrcene from geraniol may be seen as a detoxification process for the monoterpene alcohol. Neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol can be used as substrates.[1] Publication Abstract from PubMedLinalool dehydratase/isomerase (Ldi), an enzyme of terpene degradation in Castellaniella defragrans, isomerizes the primary monoterpene alcohol geraniol into the tertiary alcohol (S)-linalool and dehydrates (S)-linalool to the alkene beta-myrcene. Here we report on the crystal structures of Ldi with and without terpene substrates, revealing a cofactor-free homopentameric enzyme. The substrates were embedded inside a hydrophobic channel between two monomers of the (alpha,alpha)6 barrel fold class and flanked by three clusters of polar residues involved in acid-base catalysis. The detailed view into the active site will guide future biotechnological applications of Ldi, in particular, for industrial butadiene and isoprene production from renewable sources. This article is protected by copyright. All rights reserved. X-ray structure of linalool dehydratase/isomerase from Castellaniella defragrans reveals enzymatic alkene synthesis.,Weidenweber S, Marmulla R, Ermler U, Harder J FEBS Lett. 2016 Apr 7. doi: 10.1002/1873-3468.12165. PMID:27062179[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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